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Article
Investigation of protein unfolding and stability by computer simulation
Biochemistry and Molecular Pharmacology Publications and Presentations
  • Wilfred F. van Gunsteren
  • P. H. Hunenberger
  • H. Kovacs
  • A. E. Mark
  • Celia A. Schiffer, University of Massachusetts Medical School
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
4-29-1995
Document Type
Article
Subjects
Amino Acid Sequence; Animals; Cattle; Chickens; Computer Simulation; Molecular Sequence Data; Muramidase; Pancreatin; Plant Proteins; *Protein Folding; Protein Structure, Secondary; Repressor Proteins; Surface-Active Agents; Trypsin Inhibitors; Viral Proteins; alpha-Amylases
Abstract
Structural, dynamic and energetic properties of proteins in solution can be studied in atomic detail by molecular dynamics computer simulation. Protein unfolding can be caused by a variety of driving forces induced in different ways: increased temperature or pressure, change of solvent composition, or protein amino acid mutation. The stability and unfolding of four different proteins (bovine pancreatic trypsin inhibitor, hen egg white lysozyme, the surfactant protein C and the DNA-binding domain of the 434 repressor) have been studied by applying the afore-mentioned driving forces and also to some artificial forces. The results give a picture of protein (in)stability and possible unfolding pathways, and are compared to experimental data where possible.
DOI of Published Version
10.1098/rstb.1995.0045
Source
Philos Trans R Soc Lond B Biol Sci. 1995 Apr 29;348(1323):49-59. Link to article on publisher's site
Related Resources
Link to Article in PubMed
PubMed ID
7770486
Citation Information
Wilfred F. van Gunsteren, P. H. Hunenberger, H. Kovacs, A. E. Mark, et al.. "Investigation of protein unfolding and stability by computer simulation" Vol. 348 Iss. 1323 (1995) ISSN: 0962-8436 (Print)
Available at: http://0-works.bepress.com.library.simmons.edu/celia_schiffer/1/